7ZHF

GPN-loop GTPase from Sulfolobus acidocaldarius closed state (GppNHp)

Summary for 7ZHF

• Entry DOI: 10.2210/pdb7zhf/pdb
• Descriptor: GTPase, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: gpn-loop, self-activating, gtpase, homodimer, unknown function
• Biological source: Sulfolobus acidocaldarius
• Total number of polymer chains: 1
• Total formula weight: 31533.88

Authors

Korf, L.,Essen, L.-O. (deposition date: 2022-04-06, release date: 2023-10-25, Last modification date: 2024-05-08)

Primary citation

Korf, L.,Ye, X.,Vogt, M.S.,Steinchen, W.,Watad, M.,van der Does, C.,Tourte, M.,Sivabalasarma, S.,Albers, S.-V.,Essen, L.-O.
Archaeal GPN-loop GTPases involve a lock-switch-rock mechanism for GTP hydrolysis.
Mbio, 14:e0085923-e0085923, 2023

PubMed Abstract: GPN-loop GTPases have been found to be crucial for eukaryotic RNA polymerase II assembly and nuclear trafficking. Despite their ubiquitous occurrence in eukaryotes and archaea, the mechanism by which these GTPases mediate their function is unknown. Our study on an archaeal representative from showed that these dimeric GTPases undergo large-scale conformational changes upon GTP hydrolysis, which can be summarized as a lock-switch-rock mechanism. The observed requirement of GPN for motility appears to be due to its large footprint on the archaeal proteome.

PubMed: 37962382
DOI: 10.1128/mbio.00859-23

Experimental method

X-RAY DIFFRACTION (1.8 Å)